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4r6q

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Revision as of 17:25, 18 January 2017

Jacalin-carbohydrate interactions. Distortion of the ligand as a determinant of affinity.

Structural highlights

4r6q is a 8 chain structure with sequence from Artocarpus integer. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Related:	1jac, 1ugw, 1ku8, 1m26, 1uh0, 1ugy, 4r6n, 4r6o, 4r6p, 4r6r
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[LECA_ARTIN] D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc (Thomsen-Friedenreich-antigen-specific lectin). Potent and selective stimulant of distinct T- and B-cell functions. Shows a unique ability to specifically recognize IgA-1 from human serum. [LECB3_ARTIN] D-galactose-specific lectin, binds the T-antigen structure Gal-beta1,3-GalNAc (Thomsen-Friedenreich-antigen-specific lectin). Potent and selective stimulant of distinct T- and B-cell functions. Shows a unique ability to specifically recognize IgA-1 from human serum.

Publication Abstract from PubMed

Jacalin is among the most thoroughly studied lectins. Its carbohydrate-binding site has also been well characterized. It has been postulated that the lower affinity of beta-galactosides for jacalin compared with alpha-galactosides is caused by steric interactions of the substituents in the former with the protein. This issue has been explored energetically and structurally using different appropriate carbohydrate complexes of jacalin. It turns out that the earlier postulation is not correct. The interactions of the substituent with the binding site remain essentially the same irrespective of the anomeric nature of the substitution. This is achieved through a distortion of the sugar ring in beta-galactosides. The difference in energy, and therefore in affinity, is caused by a distortion of the sugar ring in beta-galactosides. The elucidation of this unprecedented distortion of the ligand as a strategy for modulating affinity is of general interest. The crystal structures also provide a rationale for the relative affinities of the different carbohydrate ligands for jacalin.

Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity.,Abhinav KV, Sharma K, Swaminathan CP, Surolia A, Vijayan M Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):324-31. doi:, 10.1107/S139900471402553X. Epub 2015 Jan 23. PMID:25664742^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Abhinav KV, Sharma K, Swaminathan CP, Surolia A, Vijayan M. Jacalin-carbohydrate interactions: distortion of the ligand molecule as a determinant of affinity. Acta Crystallogr D Biol Crystallogr. 2015 Feb;71(Pt 2):324-31. doi:, 10.1107/S139900471402553X. Epub 2015 Jan 23. PMID:25664742 doi:http://dx.doi.org/10.1107/S139900471402553X

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4r6q"

@@ Line 1: / Line 1: @@
 ==Jacalin-carbohydrate interactions. Distortion of the ligand as a determinant of affinity.==
 <StructureSection load='4r6q' size='340' side='right' caption='[[4r6q]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NBZ:NITROBENZENE'>NBZ</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jac|1jac]], [[1ugw|1ugw]], [[1ku8|1ku8]], [[1m26|1m26]], [[1uh0|1uh0]], [[1ugy|1ugy]], [[4r6n|4r6n]], [[4r6o|4r6o]], [[4r6p|4r6p]], [[4r6r|4r6r]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r6q OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r6q RCSB], [http://www.ebi.ac.uk/pdbsum/4r6q PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r6q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r6q OCA], [http://pdbe.org/4r6q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4r6q RCSB], [http://www.ebi.ac.uk/pdbsum/4r6q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4r6q ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 17: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4r6q" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Agglutinin|Agglutinin]]
 == References ==
 <references/>

4r6q

From Proteopedia

Revision as of 17:25, 18 January 2017

Jacalin-carbohydrate interactions. Distortion of the ligand as a determinant of affinity.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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